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Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing Epitopes
Open accessAbstract
Respiratory syncytial virus (RSV) causes severe respiratory infections in infants, young children, and the elderly, and currently, no licensed vaccine exists. In this study, we describe the crystal structure of the RSV surface glycoprotein G in complex with a broadly neutralizing human monoclonal antibody. The antibody binds to RSV G at a highly conserved region stabilized by two disulfide bonds, but it captures RSV G in a conformation not previously observed, revealing that this region is both structured and flexible. Importantly, our findings provide insight for the design of vaccines that elicit diverse antibodies, which may provide broad protection from infection and disease.
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“Broadly neutralizing human monoclonal antibody binding to conformational epitopes has been also described in other infectious disease pathogens such as respiratory syncytial virus (RSV) [22].”
From A conformational epitope in placental malaria vaccine antigen VAR2CSA: What does it teach us? (2023) · cites this paper as [22]
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A conformational epitope in placental malaria vaccine antigen VAR2CSA: What does it teach us?
Doritchamou, J. Y. A., Renn, J. P., Hviid, L., & Duffy, P. E. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011370 · Cited by 8
“Broadly neutralizing human monoclonal antibody binding to conformational epitopes has been also described in other infectious disease pathogens such as respiratory syncytial virus (RSV) [22].”
Background
Metadata
- Authors
- Fedechkin, S. O., George, N. L., Nuñez Castrejon, A. M., Dillen, J. R., Kauvar, L. M., & DuBois, R. M.
- Affiliations
- University of California, Santa Cruz (US)
- Department of Biomolecular Engineering, University of California—Santa Cruz, Santa Cruz, California, USA
- Trellis Bioscience (United States) (US)
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2020-02-28
- Volume
- 94
- Issue
- 6
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC7158734
- OpenAlex
- W2995687198
- Cited by
- 26
- References
- 4
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 3 · 2021: 5 · 2020: 1
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (R21AI130605, R56AI141537, 5R44AI122360-02)
- Topics
- Health Sciences › Medicine › Epidemiology › Respiratory viral infections research
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- respiratory syncytial virus, glycoprotein G, broadly neutralizing antibodies, monoclonal antibodies, conformational flexibility, disulfide bonds, immune complexes, crystal structure, vaccine design, antibody diversity
- MeSH terms
- CX3C Chemokine Receptor 1, Antibodies, Monoclonal, Antibodies, Viral, Epitopes, Humans, Models, Molecular, Mutation, Protein Conformation, Viral Fusion Proteins, Respiratory Syncytial Virus, Human, Crystallography, X-Ray, Antibodies, Neutralizing
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